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Dynamic Forcing, a Method for Evaluating Activity and Selectivity Profiles of RGD (Arg‐Gly‐Asp) Peptides
Author(s) -
Müller Gerhard,
Gurrath Marion,
Kessler Horst,
Timpl Rupert
Publication year - 1992
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199203261
Subject(s) - selectivity , forcing (mathematics) , receptor , chemistry , molecular dynamics , stereochemistry , peptide , biophysics , computational chemistry , biochemistry , physics , biology , atmospheric sciences , catalysis
The easy interconversion between two conformations , which is deduced from molecular dynamics simulations, explains why the cyclopeptide 1 is equally well bound to two receptors whereas the very similar cyclopeptide 2 shows a selectivity towards these receptors of ca. 30:1. The method of “dynamic forcing” showed that 1 can very easily be transformed from its most stable conformation into a conformation which corresponds to that of 2 . Thus, for the first time a connection between the biological activity of a compound and its conformational freedom has been established.